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Protein

Beta-lactamase 2

Gene
N/A
Organism
Bacillus cereus
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Can hydrolyze carbapenem compounds.

Catalytic activityi

A beta-lactam + H2O = a substituted beta-amino acid.

Cofactori

Zn2+Note: Binds 2 Zn2+ ions per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi115 – 1151Zinc 1By similarity
Metal bindingi117 – 1171Zinc 1By similarity
Metal bindingi119 – 1191Zinc 2By similarity
Metal bindingi178 – 1781Zinc 1By similarity
Metal bindingi197 – 1971Zinc 2By similarity
Metal bindingi239 – 2391Zinc 2By similarity

GO - Molecular functioni

  1. beta-lactamase activity Source: UniProtKB-EC
  2. zinc ion binding Source: InterPro

GO - Biological processi

  1. antibiotic catabolic process Source: InterPro
  2. response to antibiotic Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Antibiotic resistance

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

SABIO-RKP14488.

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-lactamase 2 (EC:3.5.2.6)
Alternative name(s):
Beta-lactamase II
Cephalosporinase
Penicillinase
OrganismiBacillus cereus
Taxonomic identifieri1396 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi110 – 1101D → N: No change in activity.
Mutagenesisi119 – 1191D → N or E: Inactivates the enzyme.
Mutagenesisi177 – 1771G → E: Inactivates the enzyme.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2929Add
BLAST
Chaini30 – 256227Beta-lactamase 2PRO_0000016943Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliP14488.
SMRiP14488. Positions 37-246.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Family and domain databases

Gene3Di3.60.15.10. 1 hit.
InterProiIPR001279. Beta-lactamas-like.
IPR001018. Beta-lactamase_class-B_CS.
[Graphical view]
PfamiPF00753. Lactamase_B. 1 hit.
[Graphical view]
SMARTiSM00849. Lactamase_B. 1 hit.
[Graphical view]
SUPFAMiSSF56281. SSF56281. 1 hit.
PROSITEiPS00743. BETA_LACTAMASE_B_1. 1 hit.
PS00744. BETA_LACTAMASE_B_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P14488-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKNTLLKLGV CVSLLGITPF VSTISSVQAE RTVEHKVIKN ETGTISISQL
60 70 80 90 100
NKNVWVHTEL GYFSGEAVPS NGLVLNTSKG LVLVDSSWDD KLTKELIEMV
110 120 130 140 150
EKKFKKRVTD VIITHAHADR IGGMKTLKER GIKAHSTALT AELAKKNGYE
160 170 180 190 200
EPLGDLQSVT NLKFGNMKVE TFYPGKGHTE DNIVVWLPQY QILAGGCLVK
210 220 230 240 250
SASSKDLGNV ADAYVNEWST SIENVLKRYG NINLVVPGHG EVGDRGLLLH

TLDLLK
Length:256
Mass (Da):28,038
Last modified:January 1, 1990 - v1
Checksum:i670F62378C355C2D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M19530 Genomic DNA. Translation: AAA22562.1.
PIRiA32017.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M19530 Genomic DNA. Translation: AAA22562.1.
PIRiA32017.

3D structure databases

ProteinModelPortaliP14488.
SMRiP14488. Positions 37-246.
ModBaseiSearch...
MobiDBiSearch...

Chemistry

ChEMBLiCHEMBL1744488.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

SABIO-RKP14488.

Family and domain databases

Gene3Di3.60.15.10. 1 hit.
InterProiIPR001279. Beta-lactamas-like.
IPR001018. Beta-lactamase_class-B_CS.
[Graphical view]
PfamiPF00753. Lactamase_B. 1 hit.
[Graphical view]
SMARTiSM00849. Lactamase_B. 1 hit.
[Graphical view]
SUPFAMiSSF56281. SSF56281. 1 hit.
PROSITEiPS00743. BETA_LACTAMASE_B_1. 1 hit.
PS00744. BETA_LACTAMASE_B_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Cloning, nucleotide sequence, and expression of the Bacillus cereus 5/B/6 beta-lactamase II structural gene."
    Lim H.M., Pene J.J., Shaw R.W.
    J. Bacteriol. 170:2873-2878(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 5/B/6.
  2. "Mutations affecting the catalytic activity of Bacillus cereus 5/B/6 beta-lactamase II."
    Lim H.M., Pene J.J.
    J. Biol. Chem. 264:11682-11687(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS.
  3. "Site-directed mutagenesis of dicarboxylic acids near the active site of Bacillus cereus 5/B/6 beta-lactamase II."
    Lim H.M., Iyer R.K., Pene J.J.
    Biochem. J. 276:401-404(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS.

Entry informationi

Entry nameiBLAB_BACCE
AccessioniPrimary (citable) accession number: P14488
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: November 26, 2014
This is version 75 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.